中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Purification, characterization and the hemolytic mechanism of the hemolysin NnTX-45 from the jellyfish Nemopilema nomurai

文献类型:期刊论文

作者Lv, Baolei1; Li, Ronggui1; Li, Guantian2; Yu, Huahua2,3; Liu, Song2,3; Li, Rongfeng2,3
刊名TOXICON
出版日期2025-11-01
卷号266页码:7
关键词Jellyfish Nemopilema nomurai NnTX-45 Pore-forming toxin
ISSN号0041-0101
DOI10.1016/j.toxicon.2025.108537
通讯作者Li, Rongfeng(rongfengli@qdio.ac.cn)
英文摘要Nemopilema nomurai, a large venomous jellyfish, caused numerous stinging incidents and even many fatal cases. The venom of N. nomurai contains various toxins, with hemolysin being one of the major components that play a crucial role in stinging. However, until now, the hemolysin has not been successfully isolated from N. nomurai, and its mechanism remains unclear. In this study, we established an improved method for preparing jellyfish toxins to facilitate subsequent purification. The SDS-PAGE profiles indicated that the crude toxin extracted using this improved method contained significantly fewer components than the traditional method. Moreover, the proteomic and toxicity analysis revealed that the refined extract still contained most of the key toxins including hemolysin, phospholipase, and other toxins. The hemolysin was then isolated from the refined jellyfish crude toxins using a two-step purification of gel filtration chromatography followed by anion-exchange chromatography. The molecular mass of this hemolysin was 45 kDa (NnTX-45) with an HC50 of approximately 30 mu g/mL. Transmission electron microscopy observations revealed that NnTX-45 formed numerous pores, each with an inner diameter of 5.65 nm and an outer diameter of 13 nm approximately, on the erythrocyte membranes. Overall, our study successfully isolated and elucidated the preliminary hemolytic mechanism of the NnTX-45 from N. nomurai, which provides a highly purified toxin antigens for the development of jellyfish antivenom to treat this jellyfish sting in the future.
WOS关键词BOX JELLYFISH ; VENOM PROTEINS ; SEA WASP ; HABU-KURAGE ; TOXIN ; STINGS
资助项目National Natural Science Founda-tion of China[41876164]
WOS研究方向Pharmacology & Pharmacy ; Toxicology
语种英语
WOS记录号WOS:001584997600002
出版者PERGAMON-ELSEVIER SCIENCE LTD
源URL[http://ir.qdio.ac.cn/handle/337002/203548]  
专题海洋研究所_实验海洋生物学重点实验室
通讯作者Li, Rongfeng
作者单位1.Qingdao Univ, Coll Life Sci, Qingdao 266071, Peoples R China
2.Chinese Acad Sci, Inst Oceanol, Ctr Ocean Mega Sci, CAS & Shandong Prov Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
3.Qingdao Marine Sci & Technol Ctr, Lab Marine Drugs & Bioprod, Qingdao 266237, Peoples R China
推荐引用方式
GB/T 7714
Lv, Baolei,Li, Ronggui,Li, Guantian,et al. Purification, characterization and the hemolytic mechanism of the hemolysin NnTX-45 from the jellyfish Nemopilema nomurai[J]. TOXICON,2025,266:7.
APA Lv, Baolei,Li, Ronggui,Li, Guantian,Yu, Huahua,Liu, Song,&Li, Rongfeng.(2025).Purification, characterization and the hemolytic mechanism of the hemolysin NnTX-45 from the jellyfish Nemopilema nomurai.TOXICON,266,7.
MLA Lv, Baolei,et al."Purification, characterization and the hemolytic mechanism of the hemolysin NnTX-45 from the jellyfish Nemopilema nomurai".TOXICON 266(2025):7.

入库方式: OAI收割

来源:海洋研究所

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